Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology最新文献

{"title":"Haemostasis and Thrombosis. Spatial Organization of the Biochemical Processes at Microscale","authors":"M. A. Panteleev,&nbsp;A. M. Shibeko,&nbsp;D. Y. Nechipurenko,&nbsp;E. A. Beresneva,&nbsp;N. A. Podoplelova,&nbsp;A. N. Sveshnikova","doi":"10.1134/S1990747822030084","DOIUrl":"10.1134/S1990747822030084","url":null,"abstract":"<p>Blood coagulation and fibrinolysis systems are enzymatic cascades in blood plasma that control formation and dissolution of a fibrin clot, respectively. However, critical processes in both systems occur on specialized scaffolds but not in the liquid phase. These scaffolds are two- or three-dimensional matrices that provide special conditions for biochemical reactions. The following fundamental categories of scaffolds can be distinguished: (a) phospholipid membranes enriched with phosphatidylserine provided by a procoagulant subpopulation of activated platelets, as well as damaged endothelium; membranes of apoptotic bodies in atherosclerotic plaque; lipoproteins and plasma microvesicles; (b) complex of fibrin and extracellular matrix proteins, which is associated with platelets and is the leading scaffold for pro- and anti-fibrinolytic processes; (c) polymers containing phosphate groups, including platelet polyphosphates and neutrophil extracellular traps. For some of these scaffolds, there are speculations about their physiological significance and physical meaning, while the role of others seems mysterious or at least pathophysiological. Herein we consider existing ideas about the roles and mechanisms of the involvement of these scaffolds in haemostasis and thrombosis.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"107 - 114"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4650128","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Presence of Azulene on the Surface of Plant Cells as a Test for Ozone Sensitivity","authors":"V. V. Roshchina,&nbsp;A. V. Kuchin,&nbsp;A. R. Kunyev,&nbsp;G. A. Soltani,&nbsp;L. M. Khaibulaeva,&nbsp;N. K. Prizova","doi":"10.1134/S1990747822010081","DOIUrl":"10.1134/S1990747822010081","url":null,"abstract":"<div><div><h3>\u0000 <b>Abstract</b>—</h3><p>The reactions to ozone of the surface cells of leaves and needles of five introduced wood species of Sochi National Park in chronic 3-day exposure in total doses of up to 0.05 μL/L have been studied. In secretory structures of silvery or ashen leaves of <i>Eucalyptus cinerea</i> F. Muell. Ex. Benth, we observed noticeable changes in absorbance (fading) and autofluorescence in cells. Blue and silvery needles of <i>Picea pungens</i> Engelm species. cv. Sv, <i>Cedrus atlantica</i> (Endl.) Manetti ex Carrière cv. Argentea, <i>Pinus parviflora</i> Siebold &amp;Zucc. Glauca and leaves of <i>Acacia dealbata</i> Link. were not sensitive to ozone in the above-mentioned reactions. It was shown that the surface layers of the cuticle and cell wall of these plants included azulenes. These pigments are supposed to be primary targets for ozone, and their antioxidant properties determine low sensitivity to ozone.</p></div></div>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"167 - 174"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4654162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"N-Terminal Fragment of Vimentin Is Responsible for Binding of Mitochondria In Vitro","authors":"A. A. Dayal,&nbsp;N. V. Medvedeva,&nbsp;A. A. Minin","doi":"10.1134/S1990747822030059","DOIUrl":"10.1134/S1990747822030059","url":null,"abstract":"<div><div><h3>\u0000 <b>Abstract</b>—</h3><p>The role of intermediate filaments in the regulation of mitochondrial functions has become evident from recent studies. For example, vimentin has been shown to affect mitochondrial motility and the level of their membrane potential. However, the mechanism of their interaction is still largely unexplored. In particular, it is unknown whether vimentin can bind directly to mitochondria or whether any intermediate proteins are needed. In this study, using bioinformatics tools, we show that the vimentin sequence has a region in the N-terminal domain, which can play the role of a mitochondrial targeting peptide that probably directs vimentin to mitochondria and causes its binding with these organelles. In order to test this possibility, the binding of mitochondria isolated from rat liver with protofilaments formed by human recombinant vimentin was investigated using centrifugation through sucrose “cushion”. We demonstrate that vimentin can bind to mitochondria in vitro. We also show that the action of a mitochondrial protease leads to the loss of the N-terminal part of the vimentin molecule and its interaction with mitochondria is disrupted. Inhibitory analysis revealed that the atypical calpain, a cysteine Ca²⁺-dependent protease that is insensitive to the inhibitor calpastatin, is responsible for its degradation.</p></div></div>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"151 - 157"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4651699","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lateral Interaction of Cylindrical Transmembrane Peptides in a One-Dimensional Approximation","authors":"O. V. Kondrashov,&nbsp;S. A. Akimov","doi":"10.1134/S1990747822030060","DOIUrl":"10.1134/S1990747822030060","url":null,"abstract":"<div><div><h3>\u0000 <b>Abstract</b>—</h3><p>Various membrane inclusions can induce deformations of lipid bilayer membranes. The characteristic length of deformation propagation along the membrane is about several nanometers. Overlapping of deformations induced by different membrane inclusions leads to their effective lateral interaction. The interaction energy can be calculated within the framework of an adequate theory of elasticity. However, in practice, such a calculation can be carried out in an analytical form only for effectively one-dimensional systems, for example, those with translational or rotational symmetry. In the general case of systems with low symmetry, the problem cannot be solved analytically. We theoretically considered the interaction of two cylindrical transmembrane peptides mediated by membrane deformations. The interaction energies were obtained by numerical minimization of the elastic energy functional. In addition, we calculated the interaction energies in a one-dimensional approximation, assuming that the system possesses the translational symmetry. It was shown that the one-dimensional approximation quite well reproduces the results of exact numerical calculations in lipid bilayers of various thicknesses and rigidities.</p></div></div>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"127 - 134"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4654154","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In Memory of Yuri Aleksandrovich Chizmadzhev 15.12.1931–05.01.2022","authors":"","doi":"10.1134/S1990747822080013","DOIUrl":"10.1134/S1990747822080013","url":null,"abstract":"","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"180 - 181"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4652570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Features of the Structure and Electrophysiological Properties of a Novel Porin from the Marine Bacterium Marinomonas primoryensis","authors":"D. K. Chistyulin,&nbsp;E. A. Zelepuga,&nbsp;V. A. Khomenko,&nbsp;O. Yu. Portnyagina,&nbsp;O. D. Novikova","doi":"10.1134/S1990747822030047","DOIUrl":"10.1134/S1990747822030047","url":null,"abstract":"<p>Using the method of protein reconstitution into planar bilayer lipid membranes, the electrophysiological properties of a novel porin channel from the marine bacterium <i>Marinomonas primoryensis</i> (MpOmp) were characterized. The main characteristics were determined: the conductivity value of the single MpOmp channel, its selectivity, and the values of the critical closing potential in various media (neutral, weakly acidic, alkaline). Using an in silico approach, the geometric characteristics of the MpOmp pore and the distribution of charges at the mouth and inside the porin channel were predicted.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"175 - 179"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4942696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Changes in Chloroplast Fluorescence Related to Excitability and Metabolite Transport by Cytoplasmic Streaming in Chara Cells","authors":"A. A. Bulychev,&nbsp;A. V. Alova","doi":"10.1134/S1990747822030035","DOIUrl":"10.1134/S1990747822030035","url":null,"abstract":"<p>Propagation of action potentials and the transfer of metabolites with the streaming cytoplasm represent two main pathways of long-distance signaling in giant cells of characean algae. This work shows that the excitation of plasma membranes and the arrest of cytoplasmic streaming in <i>Chara</i> cells at low light (in the absence of large pH changes on the cell surface) is accompanied by a transient increase or a series of oscillations of chlorophyll <i>F</i> ' fluorescence in chloroplasts located near zones of external calcification but has no effect on fluorescence of chloroplasts in the predominant non-calcified cell areas. The different sensitivity to the action potential generation in chloroplasts located near and far from the incrustation zones is probably due to structural and biochemical differences of cellular domains and to the influence of cytoplasmic streaming on chloroplast environment in the area of fluorescence measurements. The kinetic curves of <i>F</i> ' changes upon cell excitation and the number of individual peaks in the <i>F</i> ' response depended on the illuminated area of plant sample. The number of peaks diminished when the overall illumination was replaced with illumination of a narrow cell region using flexible light guides with diameters of 2.0 and 0.4 mm. The results indicate that the initial stages of <i>F</i> ' changes induced by the action potential generation are caused by internal processes in chloroplasts, while the subsequent changes in <i>F</i> ' are due to the influx of metabolites from the recovering cytoplasmic flow into the chloroplasts of the studied zone. The amplitude of excitation-induced <i>F</i> ' changes decreased transiently after the transition from general to local illumination, which is explained by the depletion of reducing equivalents in the cytoplasm during postillumination CO₂ fixation under cessation of NADPH photoproduction outside the narrow illuminated zone.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"135 - 143"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4652561","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Use of Quinolizidine Derivatives of Coumarin in the Studies of the Mechanisms of Action of the Cytochrome c–Cardiolipin Complex","authors":"L. A. Romodin,&nbsp;N. P. Lysenko,&nbsp;T. N. Pashovkin","doi":"10.1134/S1990747822020064","DOIUrl":"10.1134/S1990747822020064","url":null,"abstract":"<p>The cytochrome <i>c</i>–cardiolipin complex plays a key role in triggering apoptosis via the mitochondrial pathway due to lipoperoxidase and quasi-lipoxygenase activities of cytochrome <i>c</i>. As a result of the formation of this complex, the conformation of cytochrome <i>c</i> changes, which acquires the properties of peroxidase enzymes capable of triggering lipid peroxidation reactions. The functions of the cytochrome <i>c</i>–cardiolipin complex are usually studied using the recording of enhanced (activated) chemiluminescence. The chemiluminescence enhancer or activator increases the luminescence intensity due to the migration of the electron excitation energy from the excited lipid peroxidation products to the activator molecules, followed by its chemiluminescence with a high quantum yield. It is advisable to use in such studies activators that enhance luminescence without a chemical reaction with the components of the system under study and keep their concentration unchanged during the reaction time. At the end of the last century, it was shown on the Fe²⁺-induced lipid peroxidation system that quinolizidine derivatives of coumarin are such compounds. The ideas about the immutability of their concentration were transferred without additional studies to systems in which lipid peroxidation is triggered by peroxidase. However, it was found in this study by spectrophotometry using a reaction catalyzed by the cytochrome <i>c</i>–cardiolipin complex as an example that quinolizidine derivatives of coumarin, coumarin-314 (quinolizidine[5,6,7-<i>gh</i>]3-ethoxycarbonylcoumarin) and coumarin-334 (quinolizidine[5,6,7-<i>gh</i>]3-acetylcoumarin), are direct participants in the enzymatic lipoperoxidase reaction. Based on a comparison of changes in the concentration of coumarin derivatives in the presence and absence of phosphatidic acid, we found that coumarin derivatives are predominantly substrates of the second reaction of the peroxidase catalytic cycle, that is, the reduction of a peroxidase ferriform with two oxidized equivalents (compound 1) to a peroxidase ferriform with one oxidized equivalent (compound 2). It was also shown that during the catalysis of a quasi-hypoxygenase reaction (in the absence of H₂O₂ in the system), peroxidase passes through a catalytic cycle by the mechanism of one-electron oxidation followed by reduction, while there is no ferriform stage of peroxidase with two oxidized equivalents (compound 1). The rate constants of the first-order reaction of the decomposition of coumarin derivatives during the enzymatic lipoperoxidase reaction were determined, and based on them, functions were derived for calculating correction coefficients that take into account the decomposition of coumarin derivatives for correcting chemiluminograms obtained in the study of the cytochrome <i>c</i>–cardiolipin complex.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 2","pages":"158 - 166"},"PeriodicalIF":0.5,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4942703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Role of Immobilized Phospholipids in the Initiation of Blood Coagulation under Flow Conditions","authors":"A. D. Megalinskiy,&nbsp;V. M. Loginova,&nbsp;A. M. Shibeko,&nbsp;F. I. Ataullakhanov,&nbsp;M. A. Panteleev,&nbsp;D. Y. Nechipurenko","doi":"10.1134/S1990747822020040","DOIUrl":"10.1134/S1990747822020040","url":null,"abstract":"<p>Localized thrombin production appears to be a key event in the hemostatic response to the vascular injury. This protein causes irreversible activation of platelets and is responsible for the formation of a fibrin mesh that stabilizes the hemostatic plug. It is generally accepted that flow has a strong inhibitory effect on the kinetics of plasma coagulation reactions, so that thrombin generation and fibrin formation are restricted to the areas, which are protected from the diluting effect of the blood flow, for example, inside the platelet aggregate or in the subendothelial matrix. However, experimental evidence indicates the possibility of in vitro fibrin polymerization at arterial shear rates in the absence of platelets. Here, using in vitro experiments and in silico models, we show that the initiation of plasma coagulation under arterial shear rates can occur due to the presence of an immobilized phospholipid fraction in the area mimicking the damaged vascular wall. Our results suggest that binding of coagulation factors to these phospholipids allows the initial stages of plasma coagulation to be protected from the flow and leads to a rapid thrombin production even under conditions of arterial blood shear rates. Thus, the obtained data suggest that under certain conditions activation of secondary hemostasis may precede and promote platelet activation and aggregation.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 1","pages":"38 - 48"},"PeriodicalIF":0.5,"publicationDate":"2022-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4569494","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functioning of the Pregnan X Receptor under Oxidative Stress","authors":"Yu. V. Abalenikhina,&nbsp;E. A. Sudakova,&nbsp;A. A. Slepnev,&nbsp;A. A. Seidkulieva,&nbsp;P. D. Erokhina,&nbsp;A. V. Shchulkin,&nbsp;E. N. Yakusheva","doi":"10.1134/S1990747822010032","DOIUrl":"10.1134/S1990747822010032","url":null,"abstract":"<p>The pregnane X receptor (PXR) is a nuclear receptor that plays an important role in regulating the expression of biotransformation and metabolism enzymes, as well as transporter proteins. There are contradictory data in the literature on the effect of oxidative stress on the amount of PXR. The purpose of this study was to evaluate the effect of oxidative stress on the functioning of PXR. The work was performed on the Caco-2 cell line. Oxidative stress was modeled with hydrogen peroxide at concentrations of 0.1, 0.5, 1, 5, 10, 50, and 100 μM and incubation duration of 3, 24, and 72 h. The amount of PXR was estimated by Western blot method. H₂O₂ at all concentrations during incubation for 3 h did not significantly affect the amount of PXR. An increase in the exposure up to 24 h at prooxidant concentrations of 10, 50, and 100 μM led to an increase in the amount of PXR, which was combined with an increase in the content of lipid peroxidation products (LPPs). Continued exposure to hydrogen peroxide for up to 72 h was accompanied by an increase in the concentration of LPPs and a decrease in the amount of PXR to control values (at the H₂O₂ concentration of 10?μM) or below it (at H₂O₂ concentrations of 50 and 100 μM). Incubation of the cells with malonic dialdehyde, the final product of lipid peroxidation, at a concentration of 10 μM for 24 h led to an increase in the amount of PXR. Thus, exposure to hydrogen peroxide for 24 h led to an increase in the amount of PXR and was associated with the inducing effect of LPPs. An increase in the exposure to 72 h leveled this inducing effect.</p>","PeriodicalId":484,"journal":{"name":"Biochemistry (Moscow), Supplement Series A: Membrane and Cell Biology","volume":"16 1","pages":"21 - 28"},"PeriodicalIF":0.5,"publicationDate":"2022-02-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4571342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}